EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.1.2.2 | 3-Fluoropyruvate | - |
Pseudomonas putida | |
5.1.2.2 | 3-hydroxypyruvate | an irreversible, time-dependent inhibitor, causes inactivation of mandelate racemase. Protection from inactivation by the competitive inhibitor benzohydroxamate. 3-Hydroxypyruvate undergoes Schiff-base formation with Lys166 at the active site, followed by formation of an aldehyde/enol(ate) adduct | Pseudomonas putida | |
5.1.2.2 | benzohydroxamate | competitive inhibitor | Pseudomonas putida | |
5.1.2.2 | mesoxalate | - |
Pseudomonas putida |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.1.2.2 | Mg2+ | dependent on | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.2.2 | Pseudomonas putida | P11444 | - |
- |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.2.2 | 1.3 | - |
3-Fluoropyruvate | pH and temperature not specified in the publication | Pseudomonas putida | |
5.1.2.2 | 1.8 | - |
mesoxalate | pH and temperature not specified in the publication | Pseudomonas putida |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.1.2.2 | evolution | mandelate racemase is a member of the enolase superfamily. The ability of the enzyme to form and deprotonate a Schiff-base intermediate furnishes a mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor | Pseudomonas putida |